期刊
JOURNAL OF BIOLOGICAL CHEMISTRY
卷 275, 期 47, 页码 36999-37005出版社
AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
DOI: 10.1074/jbc.M003430200
关键词
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资金
- NCI NIH HHS [CA75205] Funding Source: Medline
E-cadherin is a transmembrane protein that mediates Ca2+-dependent cell-cell adhesion. Cdc42, a member of the Rho family of small GTPases, participates in cytoskeletal rearrangement and cell cycle progression. Recent evidence reveals that members of the Rho family modulate E-cadherin function. To further examine the role of Cdc42 in E-cadherin-mediated cell-cell adhesion, we developed an assay for active Cdc42 using the GTPase-binding domain of the Wiskott-Aldrich syndrome protein. Initiation of E cadherin-mediated cell-cell attachment significantly increased in a time-dependent manner the amount of active Cdc42 in MCF-7 epithelial cell lysates. By contrast, Cdc42 activity was not increased under identical conditions in MCF-7 cells incubated with anti-E-cadherin antibodies nor in MDA-MB-231 (E-cadherin negative) epithelial cells. By fusing the Wiskott-Aldrich syndrome protein/GTPase-binding domain to a green fluorescent protein, activation of endogenous Cdc42 by E-cadherin was demonstrated in live cells. These data indicate that E-cadherin activates Cdc42, demonstrating bi-directional interactions between the Rho- and E-cadherin signaling pathways.
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